1LRH

Crystal structure of auxin-binding protein 1 in complex with 1-naphthalene acetic acid

Summary for 1LRH

• Entry DOI: 10.2210/pdb1lrh/pdb
• Related: 1LR5
• Descriptor: auxin-binding protein 1, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (5 entities in total)
• Functional Keywords: beta jellyroll, double stranded parallel beta helix, germin like protein, protein binding
• Biological source: Zea mays
• Cellular location: Endoplasmic reticulum lumen : P13689
• Total number of polymer chains: 4
• Total formula weight: 78945.56

Authors

Woo, E.J.,Marshall, J.,Bauly, J.,Chen, J.-G.,Venis, M.,Napier, R.M.,Pickersgill, R.W. (deposition date: 2002-05-15, release date: 2002-06-19, Last modification date: 2021-11-10)

Primary citation

Woo, E.J.,Marshall, J.,Bauly, J.,Chen, J.G.,Venis, M.,Napier, R.M.,Pickersgill, R.W.
Crystal structure of auxin-binding protein 1 in complex with auxin.
EMBO J., 21:2877-2885, 2002

PubMed Abstract: The structure of auxin-binding protein 1 (ABP1) from maize has been determined at 1.9 A resolution, revealing its auxin-binding site. The structure confirms that ABP1 belongs to the ancient and functionally diverse germin/seed storage 7S protein superfamily. The binding pocket of ABP1 is predominantly hydrophobic with a metal ion deep inside the pocket coordinated by three histidines and a glutamate. Auxin binds within this pocket, with its carboxylate binding the zinc and its aromatic ring binding hydrophobic residues including Trp151. There is a single disulfide between Cys2 and Cys155. No conformational rearrangement of ABP1 was observed when auxin bound to the protein in the crystal, but examination of the structure reveals a possible mechanism of signal transduction.

PubMed: 12065401
DOI: 10.1093/emboj/cdf291

Experimental method

X-RAY DIFFRACTION (1.9 Å)